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  Protein Correlation Profiles Identify Lipid Droplet Proteins with High Confidence

Krahmer, N., Hilger, M., Kory, N., Wilfling, F., Stoehr, G., Mann, M., et al. (2013). Protein Correlation Profiles Identify Lipid Droplet Proteins with High Confidence. MOLECULAR & CELLULAR PROTEOMICS, 12(5), 1115-1126. doi:10.1074/mcp.M112.020230.

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 Creators:
Krahmer, Natalie1, Author              
Hilger, Maximiliane2, Author              
Kory, Nora1, Author
Wilfling, Florian1, Author
Stoehr, Gabriele2, Author              
Mann, Matthias2, Author              
Farese Jr., Robert V.1, Author
Walther, Tobias C.1, Author              
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: SPECTROMETRY-BASED PROTEOMICS; QUANTITATIVE PROTEOMICS; ENDOPLASMIC-RETICULUM; DROSOPHILA; SILAC; MITOCHONDRIA; MEMBRANE; REVEALS; QUANTIFICATION; TRANSLOCATION
 Abstract: Lipid droplets (LDs) are important organelles in energy metabolism and lipid storage. Their cores are composed of neutral lipids that form a hydrophobic phase and are surrounded by a phospholipid monolayer that harbors specific proteins. Most well-established LD proteins perform important functions, particularly in cellular lipid metabolism. Morphological studies show LDs in close proximity to and interacting with membrane-bound cellular organelles, including the endoplasmic reticulum, mitochondria, peroxisomes, and endosomes. Because of these close associations, it is difficult to purify LDs to homogeneity. Consequently, the confident identification of bona fide LD proteins via proteomics has been challenging. Here, we report a methodology for LD protein identification based on mass spectrometry and protein correlation profiles. Using LD purification and quantitative, high-resolution mass spectrometry, we identified LD proteins by correlating their purification profiles to those of known LD proteins. Application of the protein correlation profile strategy to LDs isolated from Drosophila S2 cells led to the identification of 111 LD proteins in a cellular LD fraction in which 1481 proteins were detected. LD localization was confirmed in a subset of identified proteins via microscopy of the expressed proteins, thereby validating the approach. Among the identified LD proteins were both well-characterized LD proteins and proteins not previously known to be localized to LDs. Our method provides a high-confidence LD proteome of Drosophila cells and a novel approach that can be applied to identify LD proteins of other cell types and tissues.

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Language(s): eng - English
 Dates: 2013-05
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000319705100006
DOI: 10.1074/mcp.M112.020230
 Degree: -

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Title: MOLECULAR & CELLULAR PROTEOMICS
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 12 (5) Sequence Number: - Start / End Page: 1115 - 1126 Identifier: ISSN: 1535-9476